Linked Life Data

7932754

Source:http://linkedlifedata.com/resource/pubmed/id/7932754

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-11-10
pubmed:abstractText
The bacteriophage P1 packaging site (pac) cleavage enzyme (pacase) consists of two phage encoded proteins, PacA and PacB. Both proteins are necessary for the recognition and cleavage of pac and for subsequent packaging of cleaved DNA into phage particles. We have purified PacA to homogeneity from a bacterial strain that overproduces the protein. Purified PacA complements an Escherichia coli extract containing the PacB protein for DNA cleavage at the pac site and recognizes and binds to methylated pac DNA independently of PacB in gel retardation experiments. The latter property of PacA is absolutely dependent on the presence of a wildtype E. coli extract, suggesting that E. coli host proteins play a role in the pac cleavage reaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
243
pubmed:geneSymbol
pacA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
258-67
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Purification and DNA-binding activity of the PacA subunit of the bacteriophage P1 pacase enzyme.
pubmed:affiliation
DuPont Merck Pharmaceutical Co. Glenolden Laboratory, PA 19036.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.